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Interleukin-18 Binding Protein (IL18BP) serves as an inhibitor of the proinflammatory cytokine, IL18. IL18BP binds IL18, inhibits the binding of IL18 to its receptor, and consequently inhibits IL18-induced IFN-gamma production, resulting in reduced T-helper type 1 immune responses. The IL18BP protein is constitutively expressed and secreted in mononuclear cells. Elevated levels of IL18BP protein are detected in the intestinal tissues of patients with Crohn's disease.

S100G (calbindin D9K) is a vitamin D-dependent calcium-binding protein. S100G, which is a cytosolic protein, is a member of a family of calcium-binding proteins that includes calmodulin, parvalbumin, troponin C, and S100 protein. In the intestine, S100G is vitamin D-dependent and its expression correlates with calcium transport activity. S100G may increase Ca2+ absorption by buffering Ca2+ in the cytoplasm and increase ATP-dependent Ca2+ transport in duodenal basolateral membrane vesicles.

Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.

Norrie Disease (NDP) is a secreted regulatory protein which activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. NDP takes part in retinal vascularization by acting as a ligand for FZD4 which signals through stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. NDP is involved in a pathway that regulates neural cell differentiation and proliferation and also in neuroectodermal cell-cell interaction.

LIN28 plays an important role as a 'translational enhancer', leading specific mRNAs to polysomes and therefore increasing the competence of protein synthesis. LIN28 is a marker of undifferentiated human embryonic stem cells and it enhances the efficiency of the formation of induced pluripotent stem (iPS) cells from human fibroblasts. LIN28 binds to the let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells. Overexpression of LIN28 is associated with human germ-cell tumors.

Human interleukin family 1, member 5 (IL-1F5 / FIL1-delta) belongs to the interleukin 1 cytokine family. IL1F5 is expressed by a variety of cells including monocytes, Bcells, dendritic cells/Langerhans cells, keratinocytes,and gastric fundus Parietal and Chief cells. IL1F5 is an antagonist of IL1F9; however IL1F5 activity related to receptor binding remains unclear. Human and mouse IL1F5 share 90% amino acid sequence identity.

UCK2 is a member of the uridinekinase family. UCK2 catalyzes the phosphorylation of uridine monophosphate to uridine diphosphate and cytidine monophosphate. UCK2 has a part in the production of pyrimidine nucleoside triphosphates essential for RNA and DNA synthesis. Furthermore, an allele of this gene is an important player in mediating nonhumoral immunity to Hemophilus influenzae type B.

PQBP1 is a transcription repressor which is connected to polyglutamine tract-containing transcription regulators and connective genes for neurodegenerative disorders. PQBP1 is restricts to the nucleus and can be found in neurons all over the brain, with high levels in hippocampus, olfactory bulb and cerebellar cortex. PQBP1 holds a WWP/WW domain that binds proline-rich motifs and a C2 domain which is able to stimulate Ca2+-dependent phospholipid signaling.

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

USP14 belongs to the ubiquitin-specific processing (UBP) family of proteases which is a deubiquitinating enzyme (DUB) containing His and Cys domains. USP14 placed in the cytoplasm and cuts the ubiquitin from ubiquitin-fused precursors and ubiquitinylated proteins.a mutation which results in reduced expression of the ortholog of USP14 in mice inhibits growth, develop severe tremors by 2 to 3 weeks of age followed by paralysis and death by 6 to 10 weeks of age.

GNG4 belongs to a multigene family and is involved in defining the specificity of receptor-G protein interaction. In mammals, G protein alpha, beta and gamma polypeptides are encoded by no less than 16, 4 and 7 genes, respectively. It is a well-known fact that different G protein complexes expressed in different tissues carry structurally distinct members of the alpha beta and gamma subunits and that privileged connotation between members of subunit families rise G protein functional diversity.

UCHL1 (PGP9.5) belongs to a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to produce the ubiquitin monomer. Protein Gene Product (PGP9.5) is a neuron specific protein, structurally and immunologically distinct from neuron specific enolase. Human UCHL1 and UCHL3 have an extremely complicated knot structure for a protein, with five knot crossings. It is considered that the knot structure may increase a protein's resistance to degradation in the proteasome.
The protein, which has a molecular weight of 27 kDa was first defined by high resolution two dimetional PAGE. Standard immunohistochemical techniques have demonstrated the presence of PGP9.5 in neurons and nerve fibers at all levels of the central and peripheral nervous system, in many neurodcrine cells, in segments of the renal tubules, in spermatogonia and leydig cells of the testis, in ova and in some cells of both the pregnant and non pregnant corpus luteum. A point mutation (I93M) in UCHL1 is implicated as the cause of Parkinson's disease in one kindred. On the other hand, a polymorphism (S18Y) in UCHL1 has been found to be associated with a reduced risk for Parkinson's disease. Furthermore, UCHL1 is associated with the Alzheimer's disease, and required for normal synaptic and cognitive function.

Tubby-related protein 1 (TULP1) belongs to the TULP family of 4 proteins (TUB and TULP1, -2, and -3), categorized structurally by the highly conserved C-terminal half of the protein. Tubby-like gene family (TULPs) members are found in plants, vertebrates, and invertebrates and encode proteins of unknown function. TULP proteins share a conserved C-terminal region of roughly 200 amino acid residues. In the retina, TULP1 is observed exclusively in the photoreceptor cells, localizing predominantly in the inner segments and connecting cilium and to a lesser degree in the perinuclear cytoplasm and synaptic termini. TULP1 gene mutations are linked with retinitis pigmentosa.

Ubiquitin thioesterase OTUB2 (OTUB2) is a member of the peptidase C65 family. OTUB2 functions as a hydrolase which can remove conjugated ubiquitin from proteins in vitro and may thus play a key regulatory role at the level of protein turnover by preventing degradation.

Ubiquitin Carboxyl-Terminal Esterase L1 (UCHL1) is a part of a family whose products hydrolyze small C-terminal adducts of ubiquitin to create the ubiquitin monomer. UCHL1 is a part of the ubiquitin system, which regulates many biological activities. UCHL1 is a thiol protease that distinguishes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 binds to free monoubiquitin and avoids its degradation in lysosomes.

RBM3 belongs to the glycine-rich RNA-binding protein family and encodes a protein with one RNArecognition motif (RRM) domain. By cold shock and low oxygen tension the expression of this gene is induced. On chromosome 1 a pseudogene exists. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.Diseases associated with RBM3 include vaccinia, andcryptorchidism. GO annotations linked to this gene include RNA binding and ribosomal large subunit binding. An important paralog of this gene is RBMY1J.

Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

Sex-hormone-binding globulin (SHBG) is a beta-globulin which specifically binds steroid hormones; it is involved in the transport of sex steroids in plasma. The main site of SHBG synthesis is assumed to be the hepatocytes. The production of SHBG is regulated by androgen/estrogen balance, thyroid hormones, insulin and dietary factors, among others. The concentration of SHBG is a key factor regulating their distribution between protein-bound and free states. SHBG concentration determination is primarily significant in the evaluation of mild disorders of androgen metabolism and it allows detection of women with hirsutism who are likely to react to estrogen therapy. Testosterone/SHBG-ratios correlate well with both measured and calculated values for free testosterone thus aid to distinguish between subjects with excessive androgen activity and normal individuals. SHBG gene polymorphisms are linked with polycystic ovary syndrome and type 2 diabetes mellitus.

Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.

RGS16 is part of the ''regulator of G protein signaling'' family. RGS16 inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. RGS16 Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha. RGS16 regulates the kinetics of signaling in the phototransduction cascade.

USP15 belongs to the ubiquitin specific protease (USP) family of deubiquitinating enzymes which has a vital role in ubiquitin-dependent processes through polyubiquitin chain disassembly and hydrolysis of ubiquitin-substrate bonds. USP15 connects with the COP9 signalosome, and takes part in transforming growth factor beta signalling through deubiquitination of receptor-activated SMAD transcription factors. Alternatively spliced transcript variants encoding multiple isoforms of this gene are known, and a pseudo gene of USP15 is sited on the long arm of chromosome 2.

Cold inducible RNA-binding protein (CIRBP) has a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. CIRBP localizes to the nucleus and contains one RRM (RNA recognition motif) domain. Expressed ubiquitously, CIRBP is believed to play a crucial role in the suppression of cellular proliferation in response to UV irradiation or extreme cold.

UFD1L forms a complex with two other proteins, nuclear protein localization-4 and valosin-containing protein, and this complex is necessary for the degradation of ubiquitinated proteins. In addition, this complex controls the disassembly of the mitotic spindle and the formation of a closed nuclear envelope after mitosis. Mutations in this gene have been associated with Catch 22 syndrome as well as cardiac and craniofacial defects. Alternative splicing results in multiple transcript variants encoding different isoforms. A related pseudogene has been identified on chromosome 18.

Sialic acid-binding Ig-like lectin 6 isoform 1 (SIGLEC6) is a member of immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family. SIGLEC6 mediates sialic-acid dependent binding to cells and binds to alpha-2, 6-linked sialic acid. The SIGLEC6 protein localizes in numerous compartments such as membrane fraction, extracellular region and so on. The SIGLEC6 receptor binds sialyl-TN glycans and leptin. Placental expression SIGLEC6 is upregulated in preeclampsia.